Abstract
The structure of d-amino acid hexapeptides that promote cellular adhesion was determined by screening d-amino acid hexapeptide libraries synthesized on otherwise inert beaded PEGA resin. These new adhesion molecules provide a completely stable cellular environment and facilitate the maintenance of a monolayer of cells on beads for extended periods. The presence of the peptides promotes spreading of the cells on the bead surface. Not surprisingly, the molecules contained a significant number of arginines and/or lysines. However, the exact structure of each peptide is quite important for the degree of adhesion observed, and a motif with three or four basic amino acids spaced within amino acids of intermediate polarity clearly prevailed, for example, k-l/r-h-r-i/v-r-a; this maintains a polar/hydrophobic balance.
Originalsprog | Engelsk |
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Tidsskrift | ChemBioChem |
Vol/bind | 12 |
Sider (fra-til) | 2463–2470 |
ISSN | 1439-4227 |
Status | Udgivet - 4 nov. 2011 |